5GWG
Solution structure of rattusin
Summary for 5GWG
| Entry DOI | 10.2210/pdb5gwg/pdb |
| NMR Information | BMRB: 36019 |
| Descriptor | Defensin alpha-related sequence 1 (1 entity in total) |
| Functional Keywords | defensin antimicrobial peptide, cysteine-rich peptide, disulfide bond, antimicrobial protein |
| Biological source | Rattus norvegicus (Rat) |
| Cellular location | Secreted : Q4JEI2 |
| Total number of polymer chains | 2 |
| Total formula weight | 7314.71 |
| Authors | |
| Primary citation | Min, H.J.,Yun, H.,Ji, S.,Rajasekaran, G.,Kim, J.I.,Kim, J.S.,Shin, S.Y.,Lee, C.W. Rattusin structure reveals a novel defensin scaffold formed by intermolecular disulfide exchanges Sci Rep, 7:45282-45282, 2017 Cited by PubMed Abstract: Defensin peptides are essential for innate immunity in humans and other living systems, as they provide protection against infectious pathogens and regulate the immune response. Here, we report the solution structure of rattusin (RTSN), an α-defensin-related peptide, which revealed a novel C-symmetric disulfide-linked dimeric structure. RTSN was synthesized by solid-phase peptide synthesis (SPPS) and refolded by air oxidation in vitro. Dimerization of the refolded RTSN (r-RTSN) resulted from five intermolecular disulfide (SS) bond exchanges formed by ten cysteines within two protomer chains. The SS bond pairings of r-RTSN were determined by mass analysis of peptide fragments cleaved by trypsin digestion. In addition to mass analysis, nuclear magnetic resonance (NMR) experiments for a C15S mutant and r-RTSN confirmed that the intermolecular SS bond structure of r-RTSN showed an I-V', II-IV', III-III', IV-II', V-I' arrangement. The overall structure of r-RTSN exhibited a cylindrical array, similar to that of β-sandwich folds, with a highly basic surface. Furthermore, fluorescence spectroscopy results suggest that r-RTSN exerts bactericidal activity by damaging membrane integrity. Collectively, these results provide a novel structural scaffold for designing highly potent peptide-based antibiotics suitable for use under various physiological conditions. PubMed: 28345637DOI: 10.1038/srep45282 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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